TY  - BOOK
AU  - Yu,Jing
ED  - SpringerLink (Online service)
TI  - Adhesive Interactions of Mussel Foot Proteins
T2  - Springer Theses, Recognizing Outstanding Ph.D. Research,
SN  - 9783319060316
AV  - TP248.3 
U1  - 660.63 23
PY  - 2014///
CY  - Cham
PB  - Springer International Publishing, Imprint: Springer
KW  - chemistry
KW  - Biochemical engineering
KW  - Biomedical engineering
KW  - Biomaterials
KW  - Surfaces (Physics)
KW  - Chemistry
KW  - Biochemical Engineering
KW  - Surfaces and Interfaces, Thin Films
KW  - Biomedical Engineering
N1  - Mussel adhesion -- Surface Interactions in Biological Systems -- Effects of interfacial redox in mussel adhesive protein films on mica -- Antioxidant is a Key Factor in Mussel Protein Adhesion -- Hydrophobic enhancement of Dopa-mediated adhesion in a mussel foot protein -- Learning from the pieces: the adhesion of mussel-inspired peptides
N2  - Water and moisture undermine strong adhesion to polar surfaces. Marine mussels, however, achieve durable underwater adhesion using a suite of proteins that are peculiar in having high levels of 3, 4-dihydroxyphenylalanine (Dopa). Mussel adhesion has inspired numerous studies on developing the next generation of wet adhesives. This thesis presents recent progress in understanding the basic surface and intermolecular interactions employed by mussels to achieve strong and durable wet adhesion. The surface forces apparatus (SFA) and various other techniques were applied to measure the interactions between mussel foot protein-3 fast (Mfp-3 fast) and the model substrate, mica, as well as the interactions between various mussel adhesive proteins. The results in this thesis show that Dopa plays an essential role in mussel adhesion, and that mussels delicately control the interfacial redox environment to achieve strong and durable Dopa mediated adhesion. The interplay between Dopa and hydrophobic interactions is also evident in mussel adhesion
UR  - http://dx.doi.org/10.1007/978-3-319-06031-6
ER  -